Compounds > 4-hydroxybenzoic acid

4-hydroxybenzoic acid and lysine

4-hydroxybenzoic acid has been researched along with lysine in 4 studies

Research

Studies (4)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's2 (50.00)18.2507
2000's2 (50.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Ballou, DP; Entsch, B; Moran, GR; Palfey, BA2
Aeschliman, SM; Ballou, DP; Massey, V; Ortiz-Maldonado, M1
Lamb, AL; Meneely, KM1

Other Studies

4 other study(ies) available for 4-hydroxybenzoic acid and lysine

ArticleYear
Evidence for flavin movement in the function of p-hydroxybenzoate hydroxylase from studies of the mutant Arg220Lys.
    Biochemistry, 1996, Jul-16, Volume: 35, Issue:28

    Topics: 4-Hydroxybenzoate-3-Monooxygenase; Arginine; Binding Sites; Catalysis; Flavin-Adenine Dinucleotide; Flavins; Hydrogen-Ion Concentration; Kinetics; Lysine; Models, Molecular; Molecular Structure; Mutagenesis, Site-Directed; Mutation; NADP; Oxidation-Reduction; Parabens; Protein Conformation; Spectrophotometry

1996
Electrostatic effects on substrate activation in para-hydroxybenzoate hydroxylase: studies of the mutant lysine 297 methionine.
    Biochemistry, 1997, Jun-17, Volume: 36, Issue:24

    Topics: 4-Hydroxybenzoate-3-Monooxygenase; Binding Sites; Catalysis; Electrochemistry; Enzyme Activation; Hydroxylation; Kinetics; Lysine; Methionine; Models, Molecular; Molecular Structure; Mutagenesis; Parabens; Structure-Activity Relationship

1997
Synergistic interactions of multiple mutations on catalysis during the hydroxylation reaction of p-hydroxybenzoate hydroxylase: studies of the Lys297Met, Asn300Asp, and Tyr385Phe mutants reconstituted with 8-Cl-flavin.
    Biochemistry, 2001, Jul-31, Volume: 40, Issue:30

    Topics: 4-Hydroxybenzoate-3-Monooxygenase; Alanine; Amino Acid Substitution; Anaerobiosis; Asparagine; Aspartic Acid; Catalysis; Flavin-Adenine Dinucleotide; Hydroxylation; Lysine; Methionine; Mutagenesis, Site-Directed; Oxidation-Reduction; Parabens; Phenylalanine; Riboflavin; Serine; Spectrophotometry; Substrate Specificity; Tyrosine

2001
Biochemical characterization of a flavin adenine dinucleotide-dependent monooxygenase, ornithine hydroxylase from Pseudomonas aeruginosa, suggests a novel reaction mechanism.
    Biochemistry, 2007, Oct-23, Volume: 46, Issue:42

    Topics: Animals; Chlorides; Enzyme Inhibitors; Flavin-Adenine Dinucleotide; Hydrogen-Ion Concentration; Hydroxylation; Kinetics; Lysine; Microsomes, Liver; Mixed Function Oxygenases; NADP; Oligopeptides; Ornithine; Oxidation-Reduction; Parabens; Pseudomonas aeruginosa; Pseudomonas fluorescens; Schizosaccharomyces; Siderophores; Solubility; Substrate Specificity; Swine

2007